| http://purl.uniprot.org/citations/11934888 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11934888 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11934888 | http://www.w3.org/2000/01/rdf-schema#comment | "Hepatitis E virus (HEV) is a human RNA virus containing three open reading frames. Of these, ORF1 encodes the viral nonstructural polyprotein; ORF2 encodes the major capsid protein, which exists in a glycosylated and non-glycosylated form; and ORF3 codes for a phosphoprotein of undefined function. Using fluorescence-based colocalization, yeast two-hybrid experiments, transiently transfected COS-1 cell co-immunoprecipitation, and cell-free coupled transcription-translation techniques, we have shown that the ORF3 protein interacts with the ORF2 protein. The domains involved in this ORF2-ORF3 association have been identified and mapped. Our deletion analysis showed that a 25-amino acid region (residues 57-81) of the ORF3 protein is required for this interaction. Using a Mexican HEV isolate, site-directed mutagenesis of ORF3, and a phosphatase digestion assay, we showed that the ORF2-ORF3 interaction is dependent upon the phosphorylation at Ser(80) of ORF3. Finally, using COS-1 cell immunoprecipitation experiments, we found that the phosphorylated ORF3 protein preferentially interacts with the non-glycosylated ORF2 protein. These findings were confirmed using tunicamycin inhibition, point mutants, and deletion mutants expressing only non-glycosylated ORF2. ORF3 maps in the structural region of the HEV genome and now interacts with the major capsid protein, ORF2, in a post-translational modification-dependent manner. Such an interaction of ORF2 with ORF3 suggests a possible well regulated role for ORF3 in HEV structural assembly."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m200185200"xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m200185200"xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Jameel S."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Jameel S."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Korkaya H."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Korkaya H."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Lal S.K."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Lal S.K."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Tyagi S."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Tyagi S."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Zafrullah M."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/author | "Zafrullah M."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/pages | "22759-22767"xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/pages | "22759-22767"xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/title | "The phosphorylated form of the ORF3 protein of hepatitis E virus interacts with its non-glycosylated form of the major capsid protein, ORF2."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/title | "The phosphorylated form of the ORF3 protein of hepatitis E virus interacts with its non-glycosylated form of the major capsid protein, ORF2."xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11934888 | http://purl.uniprot.org/core/volume | "277"xsd:string |